Dataset Information

N-Glycome and N-Glycoproteome of a Hematophagous Parasitic Nematode Haemonchus

ABSTRACT: N-glycosylation is a physiologically vital post-translational modification of proteins in eukaryotic organisms. Initial work on Haemonchus contortus – an economically-important blood-sucking nematode of ruminants with a broad geographical distribution – has shown that the parasite harbors N-glycans with exclusive core chitobiose modifications, and severel immunogenic proteins (e.g., amino- and metallo-peptidases) in the adult worms are N-glycosylated. However, an informative atlas of N-glycosylation in H. contortus is not yet available. Herein, we report a total of 291 N-glycosylated proteins with 425 sites in this parasite. Functional analyses of glycoproteome revealed significant enrichment of the peptidase families (e.g., peptidase C1 and M1), many of which are potential vaccine targets. Besides, the glycan-rich conjugates are distributed primarily in the intestine and gonads of the adult worms. These data, taken together, provide a comprehensive insight into the N-glycosylation of a prevalent parasitic nematode, while underlining its significance for the infection and prophylaxis.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Haemonchus Contortus (barber Pole Worm)

TISSUE(S): Whole Body

SUBMITTER: Chunqun Wang

LAB HEAD: Min Hu

PROVIDER: PXD023379 | Pride | 2021-09-09

REPOSITORIES: Pride

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N-glycome and N-glycoproteome of a hematophagous parasitic nematode Haemonchus.

Wang Chunqun C Gao Wenjie W Yan Shi S Zhu Xing-Quan XQ Suo Xun X Liu Xin X Gupta Nishith N Hu Min M

Computational and structural biotechnology journal 20210418

N-glycosylation is a physiologically vital post-translational modification of proteins in eukaryotic organisms. Initial work on Haemonchus contortus - a blood-sucking nematode of ruminants with a broad geographical distribution - has shown that this parasite harbors N-glycans with exclusive chitobiose modifications. Besides, several immunogenic proteins (e.g., amino- and metallo-peptidases) are known to be N-glycosylated in adult worms. However, an informative atlas of N-glycosylat ...[more]

PMID: 34025939

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Project description:Ovarian cancer is one of the most common cancer among women in the world, and chemotherapy remains the principal treatment for patients. However, drug resistance is a major obstacle to the effective treatment of ovarian cancers and the underlying mechanism is not clear. An increased understanding of the mechanisms that underline the pathogenesis of drug resistance is therefore needed to develop novel therapeutics and diagnostic. Herein, we report the comparative analysis of the doxorubicin sensitive OVCAR8 cells and its doxorubicin-resistant variant NCI/ADR-RES cells using integrated global proteomics and N-glycoproteomics. A total of 1525 unique N-glycosite-containing peptides from 740 N-glycoproteins were identified and quantified, of which 253 N-glycosite-containing peptides showed significant change in the NCI/ADR-RES cells. Meanwhile, stable isotope labeling by amino acids in cell culture (SILAC) based comparative proteomic analysis of the two ovarian cancer cells led to the quantification of 5509 proteins. As about 50% of the identified N-glycoproteins are low-abundance membrane proteins, only 44% of quantified unique N-glycosite-containing peptides had corresponding protein expression ratios. The comparison and calibration of the N-glycoproteome versus the proteome classified 14 change patterns of N-glycosite-containing peptides, including 8 up-regulated N-glycosite-containing peptides with the increased glycosylation sites occupancy, 35 up-regulated N-glycosite-containing peptides with the unchanged glycosylation sites occupancy, 2 down-regulated N-glycosite-containing peptides with the decreased glycosylation sites occupancy, 46 down-regulated N-glycosite-containing peptides with the unchanged glycosylation sites occupancy. Integrated proteomic and N-glycoproteomic analyses provide new insights, which can help to unravel the relationship of N-glycosylation and multidrug resistance (MDR), understand the mechanism of MDR, and discover the new diagnostic and therapeutic targets.

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Dataset Information

N-Glycome and N-Glycoproteome of a Hematophagous Parasitic Nematode Haemonchus

Dataset's files

Publications

N-glycome and N-glycoproteome of a hematophagous parasitic nematode <i>Haemonchus</i>.

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